Bacillus subtilis Ser/Thr/Tyr 70:20:10 Human HeLa cell culture Ser/Thr/Tyr 86:12:2
||Macek B. The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol Cell Proteomics. 2007 Apr6(4):697-707 p.703 right column 2nd paragraphPubMed ID17218307
|| Olsen, J. V. et al., (2006) Global, in-vivo and site-specific phosphorylation dynamics of signaling networks. Cell 127, 635– 648PubMed ID17081983
||p.698 left column 3rd paragraph:"In this study [investigators] enzymatically digested the entire B. subtilis proteome and enriched phosphopeptides by titanium oxide chromatography (ref 42). Phosphopeptides were measured in a hybrid linear ion trap-Fourier transform ion cyclotron resonance or an orbitrap mass spectrometer, which determines their mass and fragmentation spectra. This gel-free approach has recently proven to be extremely powerful in studies of eukaryotic protein phosphorylation and allowed the determination of more than 6600 phosphorylation sites in HeLa cells (primary source 43). Here [investigators] used this technology to obtain a site-specific, in vivo phosphoproteome of B. subtilis."
||p.703 right column 2nd paragraph:"Tyrosine phosphorylation in eukaryotes is usually thought to have arisen in connection with multicellularity, and accordingly metazoans have a higher proportion than unicellular eukaryotes such as S. cerevisiae, which has very few tyrosine sites. An interesting observation that emerges directly from [investigators’] data is the relatively high extent of tyrosine phosphorylation. [Investigators] found a ratio of 70:20:10 for Ser/Thr/Tyr in B. subtilis, more similar to metazoans than to yeast. For example, [they] have recently found this ratio to be 86:12:2 in human cell culture (primary source 43)."